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lüll Prion diseases of humans and farm animals: epidemiology, genetics, and pathogenesis Aguzzi AJ Neurochem 2006[Jun]; 97 (6): 1726-39Neuronal vacuolation (spongiosis), neuronal death, and pronounced glial reactions are the hallmarks of transmissible spongiform encephalopathies (TSEs), or prion diseases. A wealth of physical, biochemical, and immunological evidence indicates that the TSE agent, termed prion, does not contain agent-specific nucleic acid encoding its own constituents, as is the case for all other infectious pathogens. Also, no adaptive immune responses are elicited upon infection. A defining feature of TSEs is the deposition, mainly in the brain and lymphoreticular tissues, of an aggregated and structurally abnormal protein, designated PrP(Sc) or PrP-res, which represents a conformational isomer of the ubiquitous surface protein PrP(C). Biochemical and genetic evidence link PrP and its gene to the disease. Although TSEs are by definition transmissible, a growing number of Prnp-associated non-infectious neurodegenerative proteinopathies are now being recognized.|*Prion Diseases/epidemiology/genetics/pathology[MESH]|Animal Diseases/epidemiology/genetics/pathology[MESH]|Animals[MESH]|Animals, Domestic[MESH]|Creutzfeldt-Jakob Syndrome/epidemiology/genetics/veterinary[MESH]|Disease Transmission, Infectious[MESH]|Humans[MESH]|Prions/*pathogenicity[MESH] |